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  • 1970-1974  (6)
  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 19 (1972), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— The monoamine oxidases (MAO) of rat pineal gland and superior cervical ganglion were compared and found to have different characteristics. The predominant enzyme in the ganglion was inhibited by low concentrations of clorgyline (0.1 μM), exhibited a lower apparent Km for tyramine than the enzyme in the pineal, was readily inactivated by trypsin, and was relatively heat-stable. In contrast, the MAO of the pineal was inhibited by 0.1 mm clorgyline, was not readily inactivated by trypsin, and was heat-labile. Moreover, these enzymes appeared to have different substrate specificities. Our results are consistent with the view that there may be multiple forms of MAO and that these forms may be associated with specific cell types.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 19 (1972), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Angiotensin converting enzyme of rat brain was studied using Hip-His-Leu as substrate. The highest specific activity of the enzyme was associated with the microsomal fraction. The specific activity of the microsomal enzyme in several regions of the rat brain varied significantly. For example, the specific activities of the striatal and pituitary enzymes were about 10-fold greater than that of the cerebral cortical enzyme. The enzyme required chloride ion; moreover, activity was inhibited in the presence of disodium EDTA or O-phenanthroline, effects suggesting that the converting enzyme of brain is a metalloprotein. SQ-20881, a nonapeptide that inhibits converting enzyme in peripheral tissue, was a potent inhibitor of the enzyme of brain. In addition to Hip-His-Leu, the microsomal fraction was capable of liberating C terminal dipeptides from angiotensin I, Hip-Gly-Gly and Z-Gly- Gly-Val. The broad substrate specificity of the enzyme suggests that, in addition to the possible contribution of the enzyme to the brain renin-angiotensin system, other naturally occurring peptides might also be substrates for the enzyme.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 21 (1973), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 21 (1973), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Phenol sulphotransferase activity in homogenates of rat liver and brain was determined spectrophotometrically. Rat liver had about 100-fold more phenol sulphotransferase activity than brain; however, both tissues showed about the same spectrum of activity towards the phenolic compounds tested. Dopamine and its acidic and neutral metabolites and the neutral metabolites of norepinephrine were the compounds most readily sulphury-lated in vitro. They were also the compounds most readily sulphurylated in vivo when they were injected intraventricularly together with labelled Na2SO4. When labelled Na2SO4 was injected alone, we detected conjugation of endogenous phenols. One of the compounds formed was identified by its chromatographic characteristics as 3-methoxy-4-hydroxy-phenylethyleneglycol sulphate. We detected other conjugates which appeared to be the sulphate esters of 3,4-dihydroxyphenylethyleneglycol; 3,4-dihydroxyphenylacetic acid; and homovanillic acid. In brain, sulphate conjugation may be a major route of metabolism for many of the phenolic compounds related to the biogenic amines and possibly for phenolic drugs which enter the brain.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 18 (1971), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: One hour after the intravenous injection of pargyline (10 mg/kg), the activity of monoamine oxidase (EC 1.4.3.4) in various brain regions, in the submaxillary gland and in the superior cervical ganglion of the rat was inhibited by about 95 per cent. From the return of monoamine oxidase activity with time, we estimated that the half-life of the enzyme is about 11 days in the brain and 4 days in the submaxillary gland and superior cervical ganglion. The return of activity was inhibited by treatment with cycloheximide. The half-life of monoamine oxidase in brain regions bore no relationship to the turnover rates of the monoamines.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 19 (1972), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: —The half-life of tryptophan 5-hydroxylase (EC 1.14.3) in rats was estimated from the return of enzyme activity after administration of p-chlorophenylalanine and from the decline of enzyme activity in spinal cord after transection or an intraspinal injection of colchicine. The half-life was 2–3 days. Axonal transport of enzyme, estimated from the reappearance of activity in consecutive portions of spinal cord after treatment with p-chlorophenylalanine, was of the order of 5–7 mm/day. This rate is characteristic of 'slow’axonal flow. Our results suggest that changes in the synthesis of new enzyme are probably not responsible for acute changes in the turnover of serotonin.
    Type of Medium: Electronic Resource
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